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Q9UK32

- KS6A6_HUMAN

UniProt

Q9UK32 - KS6A6_HUMAN

Protein

Ribosomal protein S6 kinase alpha-6

Gene

RPS6KA6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Constitutively activated by phosphorylation at Ser-232, Ser-372, and Ser-389 in serum-starved cells. Does not require growth factor stimulation for significant kinase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei105 – 1051ATPPROSITE-ProRule annotation
    Active sitei198 – 1981Proton acceptorBy similarity
    Binding sitei455 – 4551ATPPROSITE-ProRule annotation
    Active sitei543 – 5431Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi79 – 879ATPPROSITE-ProRule annotation
    Nucleotide bindingi432 – 4409ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. magnesium ion binding Source: InterPro
    3. protein kinase activity Source: ProtInc
    4. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. central nervous system development Source: ProtInc
    3. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
    4. negative regulation of embryonic development Source: UniProtKB
    5. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
    6. negative regulation of mesoderm development Source: UniProtKB
    7. signal transduction Source: ProtInc
    8. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_20510. RSK activation.
    REACT_20568. CREB phosphorylation through the activation of Ras.
    REACT_22365. Recycling pathway of L1.
    SignaLinkiQ9UK32.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal protein S6 kinase alpha-6 (EC:2.7.11.1)
    Short name:
    S6K-alpha-6
    Alternative name(s):
    90 kDa ribosomal protein S6 kinase 6
    Short name:
    p90-RSK 6
    Short name:
    p90RSK6
    Ribosomal S6 kinase 4
    Short name:
    RSK-4
    pp90RSK4
    Gene namesi
    Name:RPS6KA6
    Synonyms:RSK4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10435. RPS6KA6.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Nucleus 1 Publication
    Note: Predominantly cytosolic.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi372 – 3721S → A: No effect on activity. 1 Publication
    Mutagenesisi389 – 3891S → A: Strongly decreases activity. 1 Publication
    Mutagenesisi581 – 5811T → A: No effect on activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34850.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745Ribosomal protein S6 kinase alpha-6PRO_0000086209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei232 – 2321Phosphoserine1 Publication
    Modified residuei372 – 3721Phosphoserine1 Publication
    Modified residuei389 – 3891Phosphoserine2 Publications
    Modified residuei581 – 5811Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated at Ser-232, Ser-372, and Ser-389 in serum-starved cells.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UK32.
    PaxDbiQ9UK32.
    PRIDEiQ9UK32.

    PTM databases

    PhosphoSiteiQ9UK32.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UK32.
    BgeeiQ9UK32.
    CleanExiHS_RPS6KA6.
    GenevestigatoriQ9UK32.

    Organism-specific databases

    HPAiHPA002852.
    HPA003904.

    Interactioni

    Subunit structurei

    Forms a complex with MAPK3/ERK1 but not with MAPK9 or MAPK14 in serum-starved cells.

    Protein-protein interaction databases

    BioGridi118144. 37 interactions.
    IntActiQ9UK32. 28 interactions.
    MINTiMINT-1424416.
    STRINGi9606.ENSP00000262752.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UK32.
    SMRiQ9UK32. Positions 21-714.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini73 – 330258Protein kinase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini331 – 40070AGC-kinase C-terminalAdd
    BLAST
    Domaini426 – 683258Protein kinase 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 2 protein kinase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ9UK32.
    KOiK04373.
    OrthoDBiEOG7B8S38.
    PhylomeDBiQ9UK32.
    TreeFamiTF313438.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR016239. Ribosomal_S6_kinase_II.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 2 hits.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000606. Ribsml_S6_kin_2. 1 hit.
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 2 hits.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 2 hits.
    PS00108. PROTEIN_KINASE_ST. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UK32-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLPFAPQDEP WDREMEVFSG GGASSGEVNG LKMVDEPMEE GEADSCHDEG    50
    VVKEIPITHH VKEGYEKADP AQFELLKVLG QGSFGKVFLV RKKTGPDAGQ 100
    LYAMKVLKKA SLKVRDRVRT KMERDILVEV NHPFIVKLHY AFQTEGKLYL 150
    ILDFLRGGDV FTRLSKEVLF TEEDVKFYLA ELALALDHLH QLGIVYRDLK 200
    PENILLDEIG HIKLTDFGLS KESVDQEKKA YSFCGTVEYM APEVVNRRGH 250
    SQSADWWSYG VLMFEMLTGT LPFQGKDRNE TMNMILKAKL GMPQFLSAEA 300
    QSLLRMLFKR NPANRLGSEG VEEIKRHLFF ANIDWDKLYK REVQPPFKPA 350
    SGKPDDTFCF DPEFTAKTPK DSPGLPASAN AHQLFKGFSF VATSIAEEYK 400
    ITPITSANVL PIVQINGNAA QFGEVYELKE DIGVGSYSVC KRCIHATTNM 450
    EFAVKIIDKS KRDPSEEIEI LMRYGQHPNI ITLKDVFDDG RYVYLVTDLM 500
    KGGELLDRIL KQKCFSEREA SDILYVISKT VDYLHCQGVV HRDLKPSNIL 550
    YMDESASADS IRICDFGFAK QLRGENGLLL TPCYTANFVA PEVLMQQGYD 600
    AACDIWSLGV LFYTMLAGYT PFANGPNDTP EEILLRIGNG KFSLSGGNWD 650
    NISDGAKDLL SHMLHMDPHQ RYTAEQILKH SWITHRDQLP NDQPKRNDVS 700
    HVVKGAMVAT YSALTHKTFQ PVLEPVAASS LAQRRSMKKR TSTGL 745
    Length:745
    Mass (Da):83,872
    Last modified:May 1, 2000 - v1
    Checksum:i5EC5AB2FA1C19DE8
    GO
    Isoform 2 (identifier: Q9UK32-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-27: MLPFAPQDEPWDREMEVFSGGGASSGE → MGLSTSAIWKNTRVEIVNPYEVKRKVK

    Note: No experimental confirmation available.

    Show »
    Length:745
    Mass (Da):84,093
    Checksum:iD8EB15DB8C280DDD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti116 – 1161D → G in CAG38803. 1 PublicationCurated
    Sequence conflicti295 – 2951F → L in CAG38803. 1 PublicationCurated
    Sequence conflicti341 – 3411R → G in CAG38803. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401Y → C in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_040637
    Natural varianti258 – 2581S → T in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040638
    Natural varianti692 – 6921D → N.1 Publication
    Corresponds to variant rs6616890 [ dbSNP | Ensembl ].
    VAR_030670

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2727MLPFA…ASSGE → MGLSTSAIWKNTRVEIVNPY EVKRKVK in isoform 2. 1 PublicationVSP_056181Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF184965 mRNA. Translation: AAF13190.1.
    CR536566 mRNA. Translation: CAG38803.1.
    AK313240 mRNA. Translation: BAG36051.1.
    AL389887, AL354653 Genomic DNA. Translation: CAC16111.2.
    AL354653, AL389887 Genomic DNA. Translation: CAD13486.2.
    CH471104 Genomic DNA. Translation: EAW98575.1.
    BC143648 mRNA. Translation: AAI43649.1.
    CCDSiCCDS14451.1.
    RefSeqiNP_055311.1. NM_014496.4.
    UniGeneiHs.234478.

    Genome annotation databases

    EnsembliENST00000262752; ENSP00000262752; ENSG00000072133.
    ENST00000543399; ENSP00000440830; ENSG00000072133.
    GeneIDi27330.
    KEGGihsa:27330.
    UCSCiuc004eej.2. human.

    Polymorphism databases

    DMDMi11133131.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF184965 mRNA. Translation: AAF13190.1 .
    CR536566 mRNA. Translation: CAG38803.1 .
    AK313240 mRNA. Translation: BAG36051.1 .
    AL389887 , AL354653 Genomic DNA. Translation: CAC16111.2 .
    AL354653 , AL389887 Genomic DNA. Translation: CAD13486.2 .
    CH471104 Genomic DNA. Translation: EAW98575.1 .
    BC143648 mRNA. Translation: AAI43649.1 .
    CCDSi CCDS14451.1.
    RefSeqi NP_055311.1. NM_014496.4.
    UniGenei Hs.234478.

    3D structure databases

    ProteinModelPortali Q9UK32.
    SMRi Q9UK32. Positions 21-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118144. 37 interactions.
    IntActi Q9UK32. 28 interactions.
    MINTi MINT-1424416.
    STRINGi 9606.ENSP00000262752.

    Chemistry

    BindingDBi Q9UK32.
    ChEMBLi CHEMBL4924.
    GuidetoPHARMACOLOGYi 1530.

    PTM databases

    PhosphoSitei Q9UK32.

    Polymorphism databases

    DMDMi 11133131.

    Proteomic databases

    MaxQBi Q9UK32.
    PaxDbi Q9UK32.
    PRIDEi Q9UK32.

    Protocols and materials databases

    DNASUi 27330.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262752 ; ENSP00000262752 ; ENSG00000072133 .
    ENST00000543399 ; ENSP00000440830 ; ENSG00000072133 .
    GeneIDi 27330.
    KEGGi hsa:27330.
    UCSCi uc004eej.2. human.

    Organism-specific databases

    CTDi 27330.
    GeneCardsi GC0XM083318.
    HGNCi HGNC:10435. RPS6KA6.
    HPAi HPA002852.
    HPA003904.
    MIMi 300303. gene.
    neXtProti NX_Q9UK32.
    PharmGKBi PA34850.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q9UK32.
    KOi K04373.
    OrthoDBi EOG7B8S38.
    PhylomeDBi Q9UK32.
    TreeFami TF313438.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_20510. RSK activation.
    REACT_20568. CREB phosphorylation through the activation of Ras.
    REACT_22365. Recycling pathway of L1.
    SignaLinki Q9UK32.

    Miscellaneous databases

    GenomeRNAii 27330.
    NextBioi 50372.
    PROi Q9UK32.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UK32.
    Bgeei Q9UK32.
    CleanExi HS_RPS6KA6.
    Genevestigatori Q9UK32.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR016239. Ribosomal_S6_kinase_II.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000606. Ribsml_S6_kin_2. 1 hit.
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 2 hits.
    PS00108. PROTEIN_KINASE_ST. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Cerebellum.
    7. Cited for: FUNCTION IN P53/TP53 SIGNALING.
    8. "Functional characterization of human RSK4, a new 90-kDa ribosomal S6 kinase, reveals constitutive activation in most cell types."
      Duemmler B.A., Hauge C., Silber J., Yntema H.G., Kruse L.S., Kofoed B., Hemmings B.A., Alessi D.R., Froedin M.
      J. Biol. Chem. 280:13304-13314(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH MAPK3, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-232; SER-372; SER-389 AND THR-581, MUTAGENESIS OF SER-372; SER-389 AND THR-581.
    9. "The RSK family of kinases: emerging roles in cellular signalling."
      Anjum R., Blenis J.
      Nat. Rev. Mol. Cell Biol. 9:747-758(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-140; THR-258 AND ASN-692.

    Entry informationi

    Entry nameiKS6A6_HUMAN
    AccessioniPrimary (citable) accession number: Q9UK32
    Secondary accession number(s): B2R854
    , B7ZL90, Q6FHX2, Q8WX28, Q9H4S6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3